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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Dec 2016.

Valosin containing protein

p97, TER ATPase
Top mentioned proteins: ATPase, Arylamine N-Acetyltransferase, Ubiquitin, CAN, V1a
Papers on p97
Role of p97/Valosin-containing protein (VCP) and Jab1/CSN5 in testicular ischaemia-reperfusion injury.
Delibasi et al., Ankara, Turkey. In J Mol Histol, Feb 2016
Furthermore, Jab1/CSN5 expression was gradually upregulated and p97/VCP expression was downregulated in IR injury according to western blotting and immunohistochemistry.
RNF4 regulates DNA double-strand break repair in a cell cycle-dependent manner.
Ann et al., Duarte, United States. In Cell Cycle, Feb 2016
In addition, we identify p97 is present in the RNF4-KAP1 interacting complex and the inhibition of p97 renders MCF7 breast cancer cells relatively more sensitive to DNA damage.
The mammalian homologue of yeast AFG1 ATPase (Lactation elevated 1) mediates degradation of nuclear-encoded complex IV subunits.
Stiburek et al., Praha, Czech Republic. In Biochem J, Feb 2016
Yeast Afg1 was shown to mediate degradation of mitochondrially-encoded complex IV subunits, and based on its similarity with CDC48 (p97/VCP) it was suggested to facilitate extraction of polytopic membrane proteins.
Structure-Activity Study of Bioisosteric Trifluoromethyl and Pentafluorosulfanyl Indole Inhibitors of the AAA ATPase p97.
Wipf et al., Pittsburgh, United States. In Acs Med Chem Lett, Jan 2016
Exploratory SAR studies of a new phenyl indole chemotype for p97 inhibition revealed C-5 indole substituent effects in the ADPGlo assay that did not fully correlate with either electronic or steric factors.
Origin and Functional Evolution of the Cdc48/p97/VCP AAA+ Protein Unfolding and Remodeling Machine.
Sauer et al., Cambridge, United States. In J Mol Biol, Jan 2016
UNASSIGNED: The AAA+ Cdc48 ATPase (alias p97 or VCP) is a key player in multiple ubiquitin-dependent cell signaling, degradation, and quality control pathways.
Targeting the AAA ATPase p97 as an Approach to Treat Cancer through Disruption of Protein Homeostasis.
Rolfe et al., Burlingame, United States. In Cancer Cell, Dec 2015
p97 is a AAA-ATPase with multiple cellular functions, one of which is critical regulation of protein homeostasis pathways.
Systematic proteomics of the VCP-UBXD adaptor network identifies a role for UBXN10 in regulating ciliogenesis.
Harper et al., Boston, United States. In Nat Cell Biol, Oct 2015
The AAA-ATPase VCP (also known as p97 or CDC48) uses ATP hydrolysis to 'segregate' ubiquitylated proteins from their binding partners.
Clipping or Extracting: Two Ways to Membrane Protein Degradation.
Lemberg et al., Heidelberg, Germany. In Trends Cell Biol, Oct 2015
While most of our understanding of this mechanism comes from studies on p97/Cdc48-mediated protein dislocation along the endoplasmic reticulum (ER)-associated degradation (ERAD) pathway, recent studies have revealed intramembrane proteolysis to be an additional mechanism that can extract transmembrane segments.
Control of p97 function by cofactor binding.
Hänzelmann et al., Würzburg, Germany. In Febs Lett, Oct 2015
p97 (also known as Cdc48, Ter94, and VCP) is an essential, abundant and highly conserved ATPase driving the turnover of ubiquitylated proteins in eukaryotes.
ESCRT-III controls nuclear envelope reformation.
Carlton et al., Bristol, United Kingdom. In Nature, Jul 2015
How annular fusion is accomplished is unknown, but it is thought to involve the p97 AAA-ATPase complex and bears a topological equivalence to the membrane fusion event that occurs during the abscission phase of cytokinesis.
Inadequate fine-tuning of protein synthesis and failure of amino acid homeostasis following inhibition of the ATPase VCP/p97.
Auner et al., London, United Kingdom. In Cell Death Dis, 2014
The ATPase valosin-containing protein (VCP; p97) is an essential regulator of protein degradation in multiple pathways and has emerged as a target for cancer therapy.
Inhibitors of the AAA+ chaperone p97.
La Clair et al., Tucson, United States. In Molecules, 2014
One promising target is p97, an ATPase associated with various cellular activities (AAA+) chaperone.
Polyubiquitylation drives replisome disassembly at the termination of DNA replication.
Gambus et al., Birmingham, United Kingdom. In Science, 2014
Here we present evidence consistent with the idea that polyubiquitylation of a replisome component (Mcm7) leads to its disassembly at the converging terminating forks because of the action of the p97/VCP/Cdc48 protein remodeler.
Cdc48 and a ubiquitin ligase drive disassembly of the CMG helicase at the end of DNA replication.
Labib et al., Dundee, United Kingdom. In Science, 2014
The Cdc48/p97 segregase then associates with ubiquitylated CMG, leading rapidly to helicase disassembly.
Proteotoxic crisis, the ubiquitin-proteasome system, and cancer therapy.
Deshaies, Pasadena, United States. In Bmc Biol, 2013
Here, I consider possible explanations for this apparently limited applicability, and discuss whether inhibiting other broadly acting components of the ubiquitin-proteasome system - including ubiquitin-activating enzyme and the AAA-ATPase p97/VCP - might be more generally effective in cancer therapy.
A genome-wide screen identifies p97 as an essential regulator of DNA damage-dependent CDT1 destruction.
Harper et al., Boston, United States. In Mol Cell, 2011
p97 is an essential regulator of DNA damage-dependent CDT1 destruction
CDC-48/p97 coordinates CDT-1 degradation with GINS chromatin dissociation to ensure faithful DNA replication.
Hoppe et al., Köln, Germany. In Mol Cell, 2011
CDC-48/p97 coordinates CDT-1 degradation with GINS chromatin dissociation to ensure faithful DNA replication
Cdc48/p97 promotes reformation of the nucleus by extracting the kinase Aurora B from chromatin.
Meyer et al., Zürich, Switzerland. In Nature, 2008
data reveal an essential pathway that regulates reformation of the nucleus after mitosis and defines ubiquitin-dependent protein extraction as a common mechanism of Cdc48/p97 activity also during nucleus formation
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